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UniProtKB/Swiss-Prot entry P37869


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ENO_BACSU
Primary accession number P37869
Secondary accession number O32249
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 83)
Name and origin of the protein
Protein name Enolase
Synonyms EC 4.2.1.11
2-phosphoglycerate dehydratase
2-phospho-D-glycerate hydro-lyase
Gene name
Name: eno
OrderedLocusNames: BSU33900
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / Marburg;
PubMed=8021172 [NCBI, ExPASy, EBI, Israel, Japan]
Leyva-Vazquez M.A., Setlow P.;
"Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis.";
J. Bacteriol. 176:3903-3910(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
PROTEIN SEQUENCE OF 2-10, AND PHOSPHORYLATION.
PubMed=1556067 [NCBI, ExPASy, EBI, Israel, Japan]
Mitchell C., Morris P.W., Vary J.C.;
"Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis.";
J. Bacteriol. 174:2474-2477(1992).
[4]
CHARACTERIZATION, AND SUBUNIT.
DOI=10.1023/A:1020790604887; PubMed=9988532 [NCBI, ExPASy, EBI, Israel, Japan]
Brown C.K., Kuhlman P.L., Mattingly S., Slates K., Calie P.J., Farrar W.W.;
"A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis.";
J. Protein Chem. 17:855-866(1998).
[5]
SUBSTRATE BINDING AT LYS-339.
STRAIN=168;
DOI=10.1016/j.jmb.2003.12.082; PubMed=15003462 [NCBI, ExPASy, EBI, Israel, Japan]
Boeel G., Pichereau V., Mijakovic I., Maze A., Poncet S., Gillet S., Giard J.-C., Hartke A., Auffray Y., Deutscher J.;
"Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?";
J. Mol. Biol. 337:485-496(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; SER-259; TYR-281 AND SER-325, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M600464-MCP200; PubMed=17218307 [NCBI, ExPASy, EBI, Israel, Japan]
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.;
"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.";
Mol. Cell. Proteomics 6:697-707(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L29475; AAA21681.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99121; CAB15395.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B69620; B69620.
RefSeq NP_391270.1; -.
3D structure databases
HSSP Q9NDH8; 1OEP. [HSSP ENTRY / PDB]
SMR P37869; 3-427, 4-428.
ModBase P37869.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3387-MON; -.
Organism-specific databases
SubtiList BG10899; eno. [Micado]
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from electronic annotation from HAMAP).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0004634; Molecular function: phosphopyruvate hydratase activity (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00318; -; 1.
PBIL [Tree]
InterPro IPR000941; Enolase.
Graphical view of domain structure.
PANTHER PTHR11902; Enolase; 1.
Pfam PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001400; Enolase; 1.
PRINTS PR00148; ENOLASE.
ProDom PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01060; eno; 1.
PROSITE PS00164; ENOLASE; 1.
BLOCKS P37869.
Genome annotation databases
GeneID 938641; -.
GenomeReviews AL009126_GR; BSU33900.
KEGG bsu:BSU33900; -.
NMPDR fig|224308.1.peg.3396; -.
Phylogenomic databases
HOGENOM P37869; -.
Other
LinkHub P37869; -.
Genome annotation databases
CMR P37869; BSU33900.
Other
ProtoNet P37869.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted; Sporulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   430  429     Enolase. PRO_0000133841
REGION   366   369  4     Substrate binding (By similarity). 
ACT_SITE   205   205        Proton donor (By similarity). 
ACT_SITE   339   339        Proton acceptor (By similarity). 
METAL   242   242        Magnesium (By similarity). 
METAL   287   287        Magnesium (By similarity). 
METAL   314   314        Magnesium (By similarity). 
BINDING   155   155        Substrate (By similarity). 
BINDING   164   164        Substrate (By similarity). 
BINDING   287   287        Substrate (By similarity). 
BINDING   314   314        Substrate (By similarity). 
BINDING   339   339        Substrate (covalent); in inhibited form. 
BINDING   390   390        Substrate (By similarity). 
MOD_RES   141   141        Phosphothreonine. 
MOD_RES   259   259        Phosphoserine. 
MOD_RES   281   281        Phosphotyrosine. 
MOD_RES   325   325        Phosphoserine. 
CONFLICT   45    45        E -> Q (in Ref. 1; AAA21681). 
Sequence information
Length: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 46581 Da [This is the MW of the unprocessed precursor] CRC64: C82B60F49D11AE68 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPYIVDVYAR EVLDSRGNPT VEVEVYTETG AFGRALVPSG ASTGEYEAVE LRDGDKDRYL 

        70         80         90        100        110        120 
GKGVLTAVNN VNEIIAPELL GFDVTEQNAI DQLLIELDGT ENKGKLGANA ILGVSMACAR 

       130        140        150        160        170        180 
AAADFLQIPL YQYLGGFNSK TLPVPMMNIV NGGEHADNNV DIQEFMIMPV GAPNFREALR 

       190        200        210        220        230        240 
MGAQIFHSLK SVLSAKGLNT AVGDEGGFAP NLGSNEEALQ TIVEAIEKAG FKPGEEVKLA 

       250        260        270        280        290        300 
MDAASSEFYN KEDGKYHLSG EGVVKTSAEM VDWYEELVSK YPIISIEDGL DENDWEGHKL 

       310        320        330        340        350        360 
LTERLGKKVQ LVGDDLFVTN TKKLSEGIKN GVGNSILIKV NQIGTLTETF DAIEMAKRAG 

       370        380        390        400        410        420 
YTAVISHRSG ETEDSTIADI AVATNAGQIK TGAPSRTDRV AKYNQLLRIE DQLAETAQYH 

       430 
GINSFYNLNK 

P37869 in FASTA format

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